ID A0A120E9J5_9BASI Unreviewed; 753 AA.
AC A0A120E9J5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Actin actin-like protein {ECO:0000313|EMBL:KWU47311.1};
GN ORFNames=RHOSPDRAFT_30730 {ECO:0000313|EMBL:KWU47311.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU47311.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU47311.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU47311.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Actins are highly conserved proteins that are involved in
CC various types of cell motility and are ubiquitously expressed in all
CC eukaryotic cells. {ECO:0000256|ARBA:ARBA00003520}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00001836};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the actin family.
CC {ECO:0000256|ARBA:ARBA00006752, ECO:0000256|RuleBase:RU000487}.
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DR EMBL; KQ954464; KWU47311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A120E9J5; -.
DR STRING; 1305733.A0A120E9J5; -.
DR OrthoDB; 10at2759; -.
DR Proteomes; UP000062823; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 2.
DR Gene3D; 3.30.420.40; -; 4.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR004001; Actin_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; ACTIN; 1.
DR PANTHER; PTHR11937:SF387; ACTIN; 1.
DR Pfam; PF00022; Actin; 2.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 2.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 4.
DR PROSITE; PS00406; ACTINS_1; 2.
DR PROSITE; PS00432; ACTINS_2; 2.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 2.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000062823}.
SQ SEQUENCE 753 AA; 83613 MW; 15886AA3B1EC93CA CRC64;
MEDEVAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKVNREKMT
QIMFETFNVP AFYVQIQAVL SLYASGRTTG MVLDSGDGVS HTVPIYEGFA LPHAIQRIDL
AGRDLTDYLI RLLMERGYPF TTSAEREVVR DIKEKLCYVA LDFEQELQTA AQSSALEKSY
ELPDGQVITI GNERFRAPEA LFQPGLIGLE AAGIHETTYN SIMKCDLDIR KDLYGNIVMS
GGTTMYAGIS DRMQKEITAL APSSMKVKIV APPERKYSVW IGGSILASLS TFQQMWISKQ
EYDESGPSIV HRKASLAPLI HEVAALVIDN GSGMCKAGFA GDDAPRAVFP SIVGRPRHQG
VMVGMGQKDS YVGDEAQSKR GILTLKYPIE HGIVTNWDDM EKIWHHTFYN ELRVAPEEHP
VLLTEAPLNP KVNREKMTQI MFETFNAPAF YVAIQAVLSL YASGRTTGIV LDSGDGVTHT
VPIYEGYALP HAILRLDLAG RDLTEYLVKI LMERGYSFTT TAEREIVRDI KEKLCYVALD
FEQEMQTAAQ SSALEKSYEL PDGQVITIGN ERFRAPEALF QPGLIGLEAA GIHETTYNSI
MKCDLDIRKD LYGNIVMSGG TTMYAGISDR MQKEITALAP SSMKVKIVAP PERKYSVWIG
GSILASLSTF QQMWISKQEY DESGPSIVHR KCF
//
